FES1_ARATH
ID FES1_ARATH Reviewed; 587 AA.
AC Q84VG7;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 2.
DT 25-MAY-2022, entry version 87.
DE RecName: Full=Protein FRIGIDA-ESSENTIAL 1;
DE AltName: Full=Zinc finger CCCH domain-containing protein 27;
DE Short=AtC3H27;
GN Name=FES1; OrderedLocusNames=At2g33835; ORFNames=T1B8;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 207-587.
RC STRAIN=cv. Columbia;
RX PubMed=12481096; DOI=10.1104/pp.010207;
RA Xiao Y.-L., Malik M., Whitelaw C.A., Town C.D.;
RT "Cloning and sequencing of cDNAs for hypothetical genes from chromosome 2
RT of Arabidopsis.";
RL Plant Physiol. 130:2118-2128(2002).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=16291783; DOI=10.1242/dev.02170;
RA Schmitz R.J., Hong L., Michaels S., Amasino R.M.;
RT "FRIGIDA-ESSENTIAL 1 interacts genetically with FRIGIDA and FRIGIDA-LIKE 1
RT to promote the winter-annual habit of Arabidopsis thaliana.";
RL Development 132:5471-5478(2005).
RN [6]
RP NOMENCLATURE.
RX PubMed=18221561; DOI=10.1186/1471-2164-9-44;
RA Wang D., Guo Y., Wu C., Yang G., Li Y., Zheng C.;
RT "Genome-wide analysis of CCCH zinc finger family in Arabidopsis and rice.";
RL BMC Genomics 9:44-44(2008).
RN [7]
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY IN THE FRI-C COMPLEX, DOMAIN,
RP AND INTERACTION WITH FRI; FLX AND RIN1.
RX PubMed=21282526; DOI=10.1105/tpc.110.075911;
RA Choi K., Kim J., Hwang H.J., Kim S., Park C., Kim S.Y., Lee I.;
RT "The FRIGIDA complex activates transcription of FLC, a strong flowering
RT repressor in Arabidopsis, by recruiting chromatin modification factors.";
RL Plant Cell 23:289-303(2011).
CC -!- FUNCTION: Transcriptional activator involved in the FRIGIDA-mediated
CC vernalization pathway, but not in the autonomous flowering pathway.
CC Acts cooperatively with FRI (FRIGIDA) or FRL1 (FRIGIDA-LIKE 1) to
CC promote FLC (FLOWERING LOCUS C) expression. Required for the
CC stabilization of the FRI-C complex. {ECO:0000269|PubMed:16291783,
CC ECO:0000269|PubMed:21282526}.
CC -!- SUBUNIT: Component of the transcription activator complex FRI-C
CC composed of FRI, FRL1, SUF4, FLX and FES1. Interacts with FLX, (via C-
CC terminus) with FRI (via C-terminus), and with RIN1, a component of the
CC SWR1 chromatin-remodeling complex. {ECO:0000269|PubMed:21282526}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16291783}.
CC -!- TISSUE SPECIFICITY: Expressed in root and shoot apices and vasculature.
CC {ECO:0000269|PubMed:16291783}.
CC -!- DOMAIN: The zinc-finger motif is essential for transcription
CC activation. {ECO:0000269|PubMed:21282526}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AK228866; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U78721; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002685; AEC08893.1; -; Genomic_DNA.
DR EMBL; AK228866; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AY208186; AAO72717.1; -; mRNA.
DR RefSeq; NP_850221.1; NM_179890.4.
DR AlphaFoldDB; Q84VG7; -.
DR SMR; Q84VG7; -.
DR BioGRID; 3298; 45.
DR IntAct; Q84VG7; 40.
DR STRING; 3702.AT2G33835.1; -.
DR iPTMnet; Q84VG7; -.
DR PaxDb; Q84VG7; -.
DR PRIDE; Q84VG7; -.
DR ProteomicsDB; 230507; -.
DR EnsemblPlants; AT2G33835.1; AT2G33835.1; AT2G33835.
DR GeneID; 817951; -.
DR Gramene; AT2G33835.1; AT2G33835.1; AT2G33835.
DR KEGG; ath:AT2G33835; -.
DR Araport; AT2G33835; -.
DR TAIR; locus:504955962; AT2G33835.
DR eggNOG; ENOG502RGRS; Eukaryota.
DR HOGENOM; CLU_018375_0_0_1; -.
DR InParanoid; Q84VG7; -.
DR OMA; AKGWCIK; -.
DR OrthoDB; 591974at2759; -.
DR PhylomeDB; Q84VG7; -.
DR PRO; PR:Q84VG7; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q84VG7; baseline and differential.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0009908; P:flower development; IEA:UniProtKB-KW.
DR GO; GO:0010220; P:positive regulation of vernalization response; IGI:TAIR.
DR InterPro; IPR000571; Znf_CCCH.
DR InterPro; IPR036855; Znf_CCCH_sf.
DR Pfam; PF00642; zf-CCCH; 1.
DR SUPFAM; SSF90229; SSF90229; 1.
DR PROSITE; PS50103; ZF_C3H1; 1.
PE 1: Evidence at protein level;
KW Developmental protein; Differentiation; DNA-binding; Flowering;
KW Metal-binding; Nucleus; Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..587
FT /note="Protein FRIGIDA-ESSENTIAL 1"
FT /id="PRO_0000371985"
FT ZN_FING 96..123
FT /note="C3H1-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT REGION 264..346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 368..421
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 467..492
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 270..325
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 375..389
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 587 AA; 64376 MW; 0542F758EB754B64 CRC64;
MSDSDMDIDD DEVEQKVQVH TIVRESELFD KPPIQASNSH NDVKRHSVTT PLDEQSKIIK
EQAFAQDNGT LPRFPAPGIP PRSFFTGGGG NEPEQKRAAL PCKFFAKGWC FNGVSCKFLH
VKENSNCTSQ QLAENSMAGN GGIRSDLERR ILDSREGVRV SQLSENGVTS LPTREDISFM
NPQRVFSSMS FVNPPGSQRV FPFNNEMRFM PSFENIRRES LKQTYGADFT DNRSLVINNA
NSFALRSSFV HEHRPSISSY LKTDMGSAGP AWTGSLSSSV PMNDRASTVG DFENGNSLSG
SGSLPTLQGV AVSSDKGAEA NTTSTKKKVS SDDWEPSEPF KASFTIPPYI LPSSDALYDP
FTDIENLGDR PLNDSLSSKG EHARKSSCQQ KDGDSASGPQ ARDCKNDDKS SSCSQNQHQE
TVARSLEAHG VVEGVATSVV DQNDTATPSK EISSATAAEN RVVLKRIKPA GHDSWHRSDG
SSYKKTKKSD EIDGEVRSDA GMKVMRLFRT AVVETIKEML KPLWREGRLT KDVHNMIVKK
AAEKVVGAAV QFHQVPTDTE SVDQYLGLSG TRIVKLVEGY VEKYGKP
